Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS1826; | |||||||||||
CAZyme ID | MGYG000004849_01272 | |||||||||||
CAZy Family | GH163 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3568; End: 6201 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH163 | 248 | 478 | 1.6e-31 | 0.8804780876494024 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam16126 | DUF4838 | 2.99e-33 | 251 | 477 | 37 | 259 | Domain of unknown function (DUF4838). This family consists of several uncharacterized proteins found in various Bacteroides and Chloroflexus species. The function of this family is unknown. |
PRK10150 | PRK10150 | 9.78e-10 | 774 | 855 | 57 | 136 | beta-D-glucuronidase; Provisional |
pfam02837 | Glyco_hydro_2_N | 2.71e-08 | 734 | 859 | 20 | 138 | Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. |
TIGR02169 | SMC_prok_A | 0.005 | 532 | 653 | 684 | 797 | chromosome segregation protein SMC, primarily archaeal type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] |
COG1196 | Smc | 0.006 | 514 | 690 | 827 | 981 | Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNK58589.1 | 1.19e-219 | 33 | 874 | 31 | 769 |
QNK58588.1 | 1.31e-210 | 31 | 874 | 47 | 784 |
BBI32737.1 | 6.72e-189 | 30 | 876 | 58 | 785 |
QNE22644.1 | 5.25e-80 | 123 | 872 | 125 | 758 |
QDU22041.1 | 1.26e-52 | 21 | 872 | 11 | 740 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6ECA_A | 2.08e-08 | 767 | 855 | 77 | 163 | Lactobacillusrhamnosus Beta-glucuronidase [Lacticaseibacillus rhamnosus],6ECA_B Lactobacillus rhamnosus Beta-glucuronidase [Lacticaseibacillus rhamnosus] |
6ED2_A | 2.47e-07 | 730 | 855 | 39 | 162 | ChainA, Glycosyl hydrolase family 2, TIM barrel domain protein [Faecalibacterium duncaniae] |
6D89_A | 2.83e-06 | 715 | 860 | 21 | 173 | Bacteroidesuniformis beta-glucuronidase 1 with N-terminal loop deletion [Bacteroides uniformis],6D89_B Bacteroides uniformis beta-glucuronidase 1 with N-terminal loop deletion [Bacteroides uniformis],6D89_C Bacteroides uniformis beta-glucuronidase 1 with N-terminal loop deletion [Bacteroides uniformis],6D89_D Bacteroides uniformis beta-glucuronidase 1 with N-terminal loop deletion [Bacteroides uniformis] |
6D1N_A | 6.49e-06 | 772 | 860 | 95 | 181 | Apostructure of Bacteroides uniformis Beta-glucuronidase 1 [Bacteroides uniformis],6D1N_B Apo structure of Bacteroides uniformis Beta-glucuronidase 1 [Bacteroides uniformis],6D41_A Bacteriodes uniformis beta-glucuronidase 1 bound to D-glucaro-1,5-lactone [Bacteroides uniformis],6D41_B Bacteriodes uniformis beta-glucuronidase 1 bound to D-glucaro-1,5-lactone [Bacteroides uniformis],6D6W_A Bacteroides uniformis beta-glucuronidase 1 bound to glucuronate [Bacteroides uniformis],6D6W_B Bacteroides uniformis beta-glucuronidase 1 bound to glucuronate [Bacteroides uniformis],6D6W_C Bacteroides uniformis beta-glucuronidase 1 bound to glucuronate [Bacteroides uniformis],6D6W_D Bacteroides uniformis beta-glucuronidase 1 bound to glucuronate [Bacteroides uniformis],6D7F_A Bacteroides uniformis beta-glucuronidase 1 bound to thiophenyl-beta-D-glucuronide [Bacteroides uniformis],6D7F_B Bacteroides uniformis beta-glucuronidase 1 bound to thiophenyl-beta-D-glucuronide [Bacteroides uniformis],6D7F_C Bacteroides uniformis beta-glucuronidase 1 bound to thiophenyl-beta-D-glucuronide [Bacteroides uniformis],6D7F_D Bacteroides uniformis beta-glucuronidase 1 bound to thiophenyl-beta-D-glucuronide [Bacteroides uniformis],6D7F_E Bacteroides uniformis beta-glucuronidase 1 bound to thiophenyl-beta-D-glucuronide [Bacteroides uniformis],6D7F_F Bacteroides uniformis beta-glucuronidase 1 bound to thiophenyl-beta-D-glucuronide [Bacteroides uniformis] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000477 | 0.998573 | 0.000221 | 0.000276 | 0.000222 | 0.000195 |
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